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PDBsum entry 3zls

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protein ligands metals links
Transferase PDB id
3zls
Jmol
Contents
Protein chain
315 a.a.
Ligands
92P
Metals
_NA
Waters ×61
PDB id:
3zls
Name: Transferase
Title: Crystal structure of mek1 in complex with fragment 6
Structure: Dual specificity mitogen-activated protein kinase 1. Chain: a. Fragment: residues 37-383. Synonym: mitogen-activated protein kinase kinase 1, map kin kinase 1, mapkk 1, mkk1, erk activator kinase 1, mapk/erk 1, mek 1. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_variant: sf21
Resolution:
2.50Å     R-factor:   0.195     R-free:   0.233
Authors: K.Amaning,M.Lowinsky,F.Vallee,V.Steier,C.Marcireau,A.Ugolini C.Delorme,G.Mccort,C.Andouche,S.Vougier,S.Llopart,N.Halland
Key ref: K.Amaning et al. (2013). The use of virtual screening and differential scanning fluorimetry for the rapid identification of fragments active against MEK1. Bioorg Med Chem Lett, 23, 3620-3626. PubMed id: 23648182 DOI: 10.1016/j.bmcl.2013.04.003
Date:
04-Feb-13     Release date:   22-May-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q02750  (MP2K1_HUMAN) -  Dual specificity mitogen-activated protein kinase kinase 1
Seq:
Struc:
393 a.a.
315 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.12.2  - Mitogen-activated protein kinase kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein = ADP + a phosphoprotein
ATP
+ protein
= ADP
+ phosphoprotein
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     protein phosphorylation   1 term 
  Biochemical function     transferase activity, transferring phosphorus-containing groups     4 terms  

 

 
    reference    
 
 
DOI no: 10.1016/j.bmcl.2013.04.003 Bioorg Med Chem Lett 23:3620-3626 (2013)
PubMed id: 23648182  
 
 
The use of virtual screening and differential scanning fluorimetry for the rapid identification of fragments active against MEK1.
K.Amaning, M.Lowinski, F.Vallee, V.Steier, C.Marcireau, A.Ugolini, C.Delorme, F.Foucalt, G.McCort, N.Derimay, C.Andouche, S.Vougier, S.Llopart, N.Halland, A.Rak.
 
  ABSTRACT  
 
We report the analysis of an in-house fragment screening campaign for the oncology target MEK1. The application of virtual screening (VS) as a primary fragment screening approach, followed by biophysical validation using differential screening fluorimetry (DSF), with resultant binding mode determination by X-ray crystallography (X-ray), is presented as the most time and cost-effective combination of in silico and in vitro methods to identify fragments. We demonstrate the effectiveness of the VS-DSF workflow for the early identification of fragments to both 'jump-start' the drug discovery project and to complement biochemical screening data.